This is a P41 renewal proposal to continue the National Biomedical Center for Advance ESR Technology (ACERT). Four principal areas of Technology Research and Development (TR&D) will be emphasized. They consist of 1) Structure of Proteins and Protein Complexes by Pulse Dipolar ESR;2) Protein and Membrane Dynamics and Protein Folding Dynamics by Time-Resolved and Two-Dimensional ESR;3) Very High-Frequency, High-Field ESR for Multi-frequency Studies of Dynamics in Proteins and Membranes and 4) ESR Microscopy for Biological and Biomedical Applications. Extensive Driven Biomedical Projects and other collaborations with biomedical researchers will greatly benefit from these TR&D's, which in turn are driven by the DBP needs for the new and improved ESR technologies. Thus, there is an important synergism amongst the TR&D's and the DBP's. The technologies being developed at ACERT are in many respects unique in the world. The extensive DBP's and collaborative/service projects at ACERT will continue to bring these modern ESR methods to the forefront of biomedical research, especially as the additional challenges are addressed in the TR&D's. This includes our plans to increase throughput of our facilities for which there are growing demands. The plans for dissemination and training address the need to bring these new technologies to other laboratories in the USA and elsewhere in addition to making the facilities available to outside scientists, publishing and advertising the results of the Center and running workshops on the new methodologies.

Public Health Relevance

This BTRC supports several NIH sponsored projects aimed at understanding and combating diseases and ailments (e.g. cancer, cardiac disease, AIDS, neurological disorders, Parkinsons, Alzheimers, Hodgkins diseases, Wernicke Encephlopathy, depressive disorders and Schizophrenia, P. aeruginosa lung infections, Ebola viral infections, and allergies) by studying their key proteins'structure and functional mechanisms.

National Institute of Health (NIH)
National Institute of General Medical Sciences (NIGMS)
Biotechnology Resource Grants (P41)
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Special Emphasis Panel (ZRG1-BCMB-K (40))
Program Officer
Friedman, Fred K
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Cornell University
Schools of Arts and Sciences
United States
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Orlando, Benjamin J; Malkowski, Michael G (2016) Substrate-selective Inhibition of Cyclooxygeanse-2 by Fenamic Acid Derivatives Is Dependent on Peroxide Tone. J Biol Chem 291:15069-81
Misra, S K; Andronenko, S I; Tipikin, D et al. (2016) Study of paramagnetic defect centers in as-grown and annealed TiO2 anatase and rutile nanoparticles by a variable-temperature X-band and high-frequency (236 GHz) EPR. J Magn Magn Mater 401:495-505
Srivastava, Madhur; Anderson, C Lindsay; Freed, Jack H (2016) A New Wavelet Denoising Method for Selecting Decomposition Levels and Noise Thresholds. IEEE Access 4:3862-3877
Dong, Min; Horitani, Masaki; Dzikovski, Boris et al. (2016) Organometallic Complex Formed by an Unconventional Radical S-Adenosylmethionine Enzyme. J Am Chem Soc 138:9755-8
Makhlynets, Olga V; Gosavi, Pallavi M; Korendovych, Ivan V (2016) Short Self-Assembling Peptides Are Able to Bind to Copper and Activate Oxygen. Angew Chem Int Ed Engl 55:9017-20
Tchaicheeyan, Oren; Freed, Jack H; Meirovitch, Eva (2016) Local Ordering at Mobile Sites in Proteins from Nuclear Magnetic Resonance Relaxation: The Role of Site Symmetry. J Phys Chem B 120:2886-98
Orlando, Benjamin J; Borbat, Peter P; Georgieva, Elka R et al. (2015) Pulsed Dipolar Spectroscopy Reveals That Tyrosyl Radicals Are Generated in Both Monomers of the Cyclooxygenase-2 Dimer. Biochemistry 54:7309-12
Tang, Shaogeng; Henne, W Mike; Borbat, Peter P et al. (2015) Structural basis for activation, assembly and membrane binding of ESCRT-III Snf7 filaments. Elife 4:
Yee, Estella F; Diensthuber, Ralph P; Vaidya, Anand T et al. (2015) Signal transduction in light-oxygen-voltage receptors lacking the adduct-forming cysteine residue. Nat Commun 6:10079
Akyuz, Nurunisa; Georgieva, Elka R; Zhou, Zhou et al. (2015) Transport domain unlocking sets the uptake rate of an aspartate transporter. Nature 518:68-73

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